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@ARTICLE{Polverini:51048,
      author       = {Polverini, E. and Cugini, G. and Annoni, F. and
                      Abbruzzetti, S. and Viappiani, C. and Gensch, T.},
      title        = {{M}olten globule formation in apomyoglobin monitored by the
                      fluorescent probe nile red},
      journal      = {Biochemistry},
      volume       = {45},
      issn         = {0006-2960},
      address      = {Columbus, Ohio},
      publisher    = {American Chemical Society},
      reportid     = {PreJuSER-51048},
      pages        = {5111 - 5121},
      year         = {2006},
      note         = {Record converted from VDB: 12.11.2012},
      abstract     = {The interaction of nile red (NR) with apomyoglobin (ApoMb)
                      in the native (pH 7) and molten globule (pH 4) states was
                      investigated using experimental and computational methods.
                      NR binds to hydrophobic locations in ApoMb with higher
                      affinity (K(d) = 25 +/- 5 microM) in the native state than
                      in the molten globule state (K(d) = 52 +/- 5 microM). In the
                      molten globule state, NR is located in a more hydrophobic
                      environment. The dye does not bind to the holoprotein,
                      suggesting that the binding site is located at the heme
                      pocket. In addition to monitoring steady-state properties,
                      the fluorescence emission of NR is capable of tracking
                      submillisecond, time-resolved structural rearrangements of
                      the protein, induced by a nanosecond pH jump. Molecular
                      dynamics simulations were run on ApoMb at neutral pH and at
                      pH 4. The structure obtained for the molten globule state is
                      consistent with the experimentally available structural
                      data. The docking of NR with the crystal structure shows
                      that the ligand binds into the binding pocket of the heme
                      group, with an orientation bringing the planar ring system
                      of NR to overlap with the position of two of the heme
                      porphyrin rings in Mb. The docking of NR with the ApoMb
                      structure at pH 4 shows that the dye binds to the heme
                      pocket with a slightly less favorable binding energy, in
                      keeping with the experimental K(d) value. Under these
                      conditions, NR is positioned in a different orientation,
                      reaching a more hydrophobic environment in agreement with
                      the spectroscopic data.},
      keywords     = {Animals / Apoproteins: chemistry / Apoproteins: metabolism
                      / Binding Sites / Computer Simulation / Fluorescent Dyes:
                      analysis / Horses / Hydrogen-Ion Concentration / Models,
                      Molecular / Myoglobin: chemistry / Myoglobin: metabolism /
                      Oxazines: analysis / Oxazines: chemistry / Protein Binding /
                      Protein Folding / Protein Structure, Tertiary / Apoproteins
                      (NLM Chemicals) / Fluorescent Dyes (NLM Chemicals) /
                      Myoglobin (NLM Chemicals) / Oxazines (NLM Chemicals) /
                      apomyoglobin (NLM Chemicals) / nile red (NLM Chemicals) / J
                      (WoSType)},
      cin          = {IBI-1},
      ddc          = {570},
      cid          = {I:(DE-Juel1)VDB57},
      pnm          = {Funktion und Dysfunktion des Nervensystems},
      pid          = {G:(DE-Juel1)FUEK409},
      shelfmark    = {Biochemistry $\&$ Molecular Biology},
      typ          = {PUB:(DE-HGF)16},
      pubmed       = {pmid:16618100},
      UT           = {WOS:000237049400004},
      doi          = {10.1021/bi051905y},
      url          = {https://juser.fz-juelich.de/record/51048},
}